Structure of a biological oxygen sensor: A new mechanism for heme-driven signal transduction

被引:333
作者
Gong, WM
Hao, B
Mansy, SS
Gonzalez, G
Gilles-Gonzalez, MA
Chan, MK
机构
[1] Ohio State Univ, Dept Biochem, Columbus, OH 43210 USA
[2] Ohio State Univ, Dept Chem, Columbus, OH 43210 USA
[3] Ohio State Univ, Ctr Plant Biotechnol, Columbus, OH 43210 USA
关键词
D O I
10.1073/pnas.95.26.15177
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
The FixL proteins are biological oxygen sensors that restrict the expression of specific genes to hypoxic conditions. FixL's oxygen detecting domain is a heme binding region that controls the activity of an attached histidine kinase. The FixL switch is regulated by binding of oxygen and other strong-field ligands. In the absence of bound ligand, the heme domain permits kinase activity. In the presence of bound ligand, this domain turns off kinase activity. Comparison of the structures of two forms of the Bradyrhizobium japonicum FixL heme domain, one in the "on" state without bound ligand and one in the "off" state with bound cyanide, reveals a mechanism of regulation by a heme that is distinct from the classical hemoglobin models. The close structural resemblance of the FixL heme domain to the photoactive yellow protein confirms the existence of a PAS structural motif but reveals the presence of an alternative regulatory gateway.
引用
收藏
页码:15177 / 15182
页数:6
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